ID   IF2P_HALS3              Reviewed;         600 AA.
AC   B0R6U5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Probable translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=OE_3800F;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
CC   -!- FUNCTION: Function in general translation initiation by promoting the
CC       binding of the formylmethionine-tRNA to ribosomes. Seems to function
CC       along with eIF-2. {ECO:0000255|HAMAP-Rule:MF_00100}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00100}.
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DR   EMBL; AM774415; CAP14464.1; -; Genomic_DNA.
DR   RefSeq; WP_010903469.1; NC_010364.1.
DR   AlphaFoldDB; B0R6U5; -.
DR   SMR; B0R6U5; -.
DR   EnsemblBacteria; CAP14464; CAP14464; OE_3800F.
DR   GeneID; 5953198; -.
DR   GeneID; 62887326; -.
DR   KEGG; hsl:OE_3800F; -.
DR   HOGENOM; CLU_002656_3_3_2; -.
DR   OMA; FRQSKPA; -.
DR   PhylomeDB; B0R6U5; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10050; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00100_A; IF_2_A; 1.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR029459; EFTU-type.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR004544; TF_aIF-2_arc.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR036925; TIF_IF2_dom3_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR43381; PTHR43381; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF14578; GTP_EFTU_D4; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50447; SSF50447; 1.
DR   SUPFAM; SSF52156; SSF52156; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00491; aIF-2; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Initiation factor; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..600
FT                   /note="Probable translation initiation factor IF-2"
FT                   /id="PRO_1000093790"
FT   DOMAIN          13..228
FT                   /note="tr-type G"
FT   REGION          22..29
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          47..51
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          84..87
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          138..141
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          140..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..208
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        142..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         22..29
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         84..88
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         138..141
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   600 AA;  64430 MW;  3D356AF39F01F5C9 CRC64;
     MPDADTTDDP GDLRTPIVAV LGHVDHGKTS LLDKIRGSAV IEGEAGAITQ HIGATAVPLD
     TVSEVAGSLV DPTEFDLPGL LFIDTPGHHS FSTLRSRGGA LADIAILVVD VNDGFQPQTE
     EAIRILKDTG TPFVVAANKI DTTPGWNPNP DAPVQGTYDD QSDRVRSDLD DALYELIGEM
     SDAGFSSDLY WRVQNFQKNV GVIPVSAETG EGVPDLLTVL MGLAQRYMKS EMEVTIDGPG
     AGTVLEVKDE QGFGTTVDVI LYDGTIRSGD TVVVGAQPEP IVTDVRALLK PGDLAEMRTE
     KRFGNVDRMQ AAAGLKVAAP DLDDAMAGAP IRVVGDRDVA DVVTEVEAEL AEVAVETGEE
     GIVVKADTLG SLEALVSALE EAEIPVMSAE VGDVAPRDVA MATTVDSEKH RVLLGFNVDV
     LPAAAENAER ESVRVFNSDV IYQLVEDYEA FVDAQEREQK EAVFDNIVRP ARFRILKDHV
     FRQNDPAVVG VEVVSGTLKR NTPVGGIEGN DLDRAGIVKG IQDQGEDVDE ARAGNRVSVS
     IDGPTVGRDI KEGDELWVDL PEKHAKVLDQ ELTSDLPADE REALKSYLDI MRKRDPFWGK